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Database: UniProt
Entry: A0A0Q5Z1F4_9BURK
LinkDB: A0A0Q5Z1F4_9BURK
Original site: A0A0Q5Z1F4_9BURK 
ID   A0A0Q5Z1F4_9BURK        Unreviewed;       271 AA.
AC   A0A0Q5Z1F4;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   RecName: Full=Septum site-determining protein MinD {ECO:0000256|ARBA:ARBA00016887};
DE   AltName: Full=Cell division inhibitor MinD {ECO:0000256|ARBA:ARBA00032845};
GN   ORFNames=ASG30_06805 {ECO:0000313|EMBL:KQT11572.1};
OS   Ramlibacter sp. Leaf400.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Ramlibacter.
OX   NCBI_TaxID=1736365 {ECO:0000313|EMBL:KQT11572.1, ECO:0000313|Proteomes:UP000051173};
RN   [1] {ECO:0000313|EMBL:KQT11572.1, ECO:0000313|Proteomes:UP000051173}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf400 {ECO:0000313|EMBL:KQT11572.1,
RC   ECO:0000313|Proteomes:UP000051173};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQT11572.1, ECO:0000313|Proteomes:UP000051173}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf400 {ECO:0000313|EMBL:KQT11572.1,
RC   ECO:0000313|Proteomes:UP000051173};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: ATPase required for the correct placement of the division
CC       site. Cell division inhibitors MinC and MinD act in concert to form an
CC       inhibitor capable of blocking formation of the polar Z ring septums.
CC       Rapidly oscillates between the poles of the cell to destabilize FtsZ
CC       filaments that have formed before they mature into polar Z rings.
CC       {ECO:0000256|ARBA:ARBA00025436}.
CC   -!- SUBUNIT: Interacts with MinC and FtsZ. {ECO:0000256|ARBA:ARBA00011626}.
CC   -!- SIMILARITY: Belongs to the ParA family. MinD subfamily.
CC       {ECO:0000256|ARBA:ARBA00010257}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KQT11572.1}.
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DR   EMBL; LMQL01000009; KQT11572.1; -; Genomic_DNA.
DR   RefSeq; WP_055895734.1; NZ_LMQL01000009.1.
DR   AlphaFoldDB; A0A0Q5Z1F4; -.
DR   STRING; 1736365.ASG30_06805; -.
DR   OrthoDB; 9773088at2; -.
DR   Proteomes; UP000051173; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   CDD; cd02036; MinD; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR002586; CobQ/CobB/MinD/ParA_Nub-bd_dom.
DR   InterPro; IPR010223; MinD.
DR   InterPro; IPR025501; MinD_FleN.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   NCBIfam; TIGR01968; minD_bact; 1.
DR   PANTHER; PTHR43384; SEPTUM SITE-DETERMINING PROTEIN MIND HOMOLOG, CHLOROPLASTIC-RELATED; 1.
DR   PANTHER; PTHR43384:SF6; SEPTUM SITE-DETERMINING PROTEIN MIND HOMOLOG, CHLOROPLASTIC-RELATED; 1.
DR   Pfam; PF01656; CbiA; 1.
DR   PIRSF; PIRSF003092; MinD; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051173}.
FT   DOMAIN          5..226
FT                   /note="CobQ/CobB/MinD/ParA nucleotide binding"
FT                   /evidence="ECO:0000259|Pfam:PF01656"
SQ   SEQUENCE   271 AA;  29463 MW;  847BDCA2ACE64FBE CRC64;
     MARIIVVTSG KGGVGKTTTS ASFASGLALA GHKTAVIDFD VGLRNLDLIM GCERRVVYDF
     VNVIQGEATL NQALIKDKHC DNLSVLAASQ TRDKEALNKE GVERVLKDLA EMGFEYIVCD
     SPAGIETGAL MAMHFADEAV VVTNPEVSSV RDSDRILGML SSKTRRAIEG KEPIKEHLLI
     TRYNPNRVDQ GQMLSLGDIQ DILRIKLIGV VPESETVLQA SNQGTPAVHL KGSDVSEAYK
     DVVDRFLGQD KPLRFVDAQK QGLLKRLFGG R
//
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